data_15019 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR assignments for a helical diacylglycerol kinase (DAGK), 40 kDa membrane protein from E. coli ; _BMRB_accession_number 15019 _BMRB_flat_file_name bmr15019.str _Entry_type original _Submission_date 2006-11-08 _Accession_date 2006-11-08 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kim 'Hak Jun' . . 2 Oxenoid Kirill . . 3 Jacob Jaison . . 4 Sonnichsen Frank D. . 5 Sanders Chuck R. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 109 "13C chemical shifts" 320 "15N chemical shifts" 109 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2006-12-06 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 7340 'thermally stable DAGK mutant' stop_ _Original_release_date 2006-12-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR assignments for a helical 40 kDa membrane protein' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15099070 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Oxenoid Kirill . . 2 Kim 'Hak Jun' . . 3 Jacob Jaison . . 4 Sonnichsen Frank . . 5 Sanders Chuck . . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_volume 126 _Journal_issue 16 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5048 _Page_last 5049 _Year 2004 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'DAGK homotrimer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'DAGK monomer 1' $DAGK 'DAGK monomer 2' $DAGK 'DAGK monomer 3' $DAGK stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'DAGK monomer 1' 1 'DAGK monomer 2' 1 'DAGK monomer 3' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_DAGK _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common DAGK _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function kinase stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 122 _Mol_residue_sequence ; MANNTTGFTRIIKAAGYSWK GLRAAWINEAAFRQEGVAVL LAVVIACWLDVDAITRVLLI SSVMLVMIVEILNSAIEAVV DRIGSEYHELSGRAKDMGSA AVLIAIIVAVITWCILLWSH FG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 0 MET 2 1 ALA 3 2 ASN 4 3 ASN 5 4 THR 6 5 THR 7 6 GLY 8 7 PHE 9 8 THR 10 9 ARG 11 10 ILE 12 11 ILE 13 12 LYS 14 13 ALA 15 14 ALA 16 15 GLY 17 16 TYR 18 17 SER 19 18 TRP 20 19 LYS 21 20 GLY 22 21 LEU 23 22 ARG 24 23 ALA 25 24 ALA 26 25 TRP 27 26 ILE 28 27 ASN 29 28 GLU 30 29 ALA 31 30 ALA 32 31 PHE 33 32 ARG 34 33 GLN 35 34 GLU 36 35 GLY 37 36 VAL 38 37 ALA 39 38 VAL 40 39 LEU 41 40 LEU 42 41 ALA 43 42 VAL 44 43 VAL 45 44 ILE 46 45 ALA 47 46 CYS 48 47 TRP 49 48 LEU 50 49 ASP 51 50 VAL 52 51 ASP 53 52 ALA 54 53 ILE 55 54 THR 56 55 ARG 57 56 VAL 58 57 LEU 59 58 LEU 60 59 ILE 61 60 SER 62 61 SER 63 62 VAL 64 63 MET 65 64 LEU 66 65 VAL 67 66 MET 68 67 ILE 69 68 VAL 70 69 GLU 71 70 ILE 72 71 LEU 73 72 ASN 74 73 SER 75 74 ALA 76 75 ILE 77 76 GLU 78 77 ALA 79 78 VAL 80 79 VAL 81 80 ASP 82 81 ARG 83 82 ILE 84 83 GLY 85 84 SER 86 85 GLU 87 86 TYR 88 87 HIS 89 88 GLU 90 89 LEU 91 90 SER 92 91 GLY 93 92 ARG 94 93 ALA 95 94 LYS 96 95 ASP 97 96 MET 98 97 GLY 99 98 SER 100 99 ALA 101 100 ALA 102 101 VAL 103 102 LEU 104 103 ILE 105 104 ALA 106 105 ILE 107 106 ILE 108 107 VAL 109 108 ALA 110 109 VAL 111 110 ILE 112 111 THR 113 112 TRP 114 113 CYS 115 114 ILE 116 115 LEU 117 116 LEU 118 117 TRP 119 118 SER 120 119 HIS 121 120 PHE 122 121 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-29 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 2KDC "Nmr Solution Structure Of E. Coli Diacylglycerol Kinase (Dagk) In Dpc Micelles" 99.18 121 100.00 100.00 3.56e-77 PDB 3ZE4 "Crystal Structure Of The Integral Membrane Diacylglycerol Kinase - Wild-type" 100.00 130 99.18 100.00 3.10e-77 PDB 4UP6 "Crystal Structure Of The Wild-type Diacylglycerol Kinase Refolded In The Lipid Cubic Phase" 100.00 130 99.18 100.00 3.10e-77 DBJ BAB38448 "diacylglycerol kinase [Escherichia coli O157:H7 str. Sakai]" 100.00 122 100.00 100.00 4.93e-78 DBJ BAE78044 "diacylglycerol kinase [Escherichia coli str. K12 substr. W3110]" 100.00 122 100.00 100.00 4.93e-78 DBJ BAG79858 "diacylglycerol kinase [Escherichia coli SE11]" 100.00 122 100.00 100.00 4.93e-78 DBJ BAI28303 "diacylglycerol kinase DgkA [Escherichia coli O26:H11 str. 11368]" 100.00 122 100.00 100.00 4.93e-78 DBJ BAI33480 "diacylglycerol kinase DgkA [Escherichia coli O103:H2 str. 12009]" 100.00 122 100.00 100.00 4.93e-78 EMBL CAP78501 "Diacylglycerol kinase [Escherichia coli LF82]" 100.00 122 99.18 99.18 4.10e-77 EMBL CAQ34391 "diacylglycerol kinase [Escherichia coli BL21(DE3)]" 100.00 122 100.00 100.00 4.93e-78 EMBL CAR01021 "diacylglycerol kinase [Escherichia coli IAI1]" 100.00 122 100.00 100.00 4.93e-78 EMBL CAR05676 "diacylglycerol kinase [Escherichia coli S88]" 100.00 122 99.18 99.18 4.10e-77 EMBL CAR10862 "diacylglycerol kinase [Escherichia coli ED1a]" 100.00 122 99.18 99.18 4.10e-77 GB AAA24394 "diglyceride kinase [Escherichia coli]" 100.00 122 100.00 100.00 4.93e-78 GB AAC43136 "diacylglycerol kinase [Escherichia coli str. K-12 substr. MG1655]" 100.00 122 100.00 100.00 4.93e-78 GB AAC77012 "diacylglycerol kinase [Escherichia coli str. K-12 substr. MG1655]" 100.00 122 100.00 100.00 4.93e-78 GB AAG59241 "diacylglycerol kinase [Escherichia coli O157:H7 str. EDL933]" 100.00 122 100.00 100.00 4.93e-78 GB AAN45585 "diacylglycerol kinase [Shigella flexneri 2a str. 301]" 100.00 122 100.00 100.00 4.93e-78 REF NP_313052 "diacylglycerol kinase [Escherichia coli O157:H7 str. Sakai]" 100.00 122 100.00 100.00 4.93e-78 REF NP_418466 "diacylglycerol kinase [Escherichia coli str. K-12 substr. MG1655]" 100.00 122 100.00 100.00 4.93e-78 REF NP_709878 "diacylglycerol kinase [Shigella flexneri 2a str. 301]" 100.00 122 100.00 100.00 4.93e-78 REF WP_000002899 "MULTISPECIES: diacylglycerol kinase [Enterobacteriaceae]" 100.00 122 99.18 99.18 4.10e-77 REF WP_000002905 "MULTISPECIES: diacylglycerol kinase [Escherichia]" 100.00 122 99.18 100.00 7.23e-78 SP P0ABN1 "RecName: Full=Diacylglycerol kinase; Short=DAGK; AltName: Full=Diglyceride kinase; Short=DGK" 100.00 122 100.00 100.00 4.93e-78 SP P0ABN2 "RecName: Full=Diacylglycerol kinase; Short=DAGK; AltName: Full=Diglyceride kinase; Short=DGK" 100.00 122 100.00 100.00 4.93e-78 SP P0ABN3 "RecName: Full=Diacylglycerol kinase; Short=DAGK; AltName: Full=Diglyceride kinase; Short=DGK" 100.00 122 100.00 100.00 4.93e-78 SP P0ABN4 "RecName: Full=Diacylglycerol kinase; Short=DAGK; AltName: Full=Diglyceride kinase; Short=DGK" 100.00 122 100.00 100.00 4.93e-78 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $DAGK 'E. coli' 562 Bacteria . Escherichia coli stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name _Details $DAGK 'recombinant technology' . Escherichia coli . pSD005 'synthetic gene' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DAGK 3 mM '[U-13C; U-15N; U-2H]' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'F Delaglio, S Grzesiek, GW Vuister, G Zhu, J Pfeifer and A Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'B Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 . pH temperature 318 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D HNCO' '3D HNCA' '3D HNCACB' '3D HN(CO)CA' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'DAGK monomer 1' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 2 ALA H H 8.041 . . 2 1 2 ALA C C 177.65 . . 3 1 2 ALA CA C 52.446 . . 4 1 2 ALA CB C 18.08 . . 5 1 2 ALA N N 123.268 . . 6 2 3 ASN H H 8.107 . . 7 2 3 ASN CA C 53.24 . . 8 2 3 ASN CB C 38.292 . . 9 2 3 ASN N N 117.691 . . 10 3 4 ASN C C 175.594 . . 11 3 4 ASN CA C 53.736 . . 12 3 4 ASN CB C 38.388 . . 13 4 5 THR H H 7.994 . . 14 4 5 THR C C 175.117 . . 15 4 5 THR CA C 62.236 . . 16 4 5 THR CB C 69.259 . . 17 4 5 THR N N 114.112 . . 18 5 6 THR H H 8.089 . . 19 5 6 THR C C 175.613 . . 20 5 6 THR CA C 62.099 . . 21 5 6 THR CB C 69.731 . . 22 5 6 THR N N 115.936 . . 23 6 7 GLY H H 8.588 . . 24 6 7 GLY C C 175.387 . . 25 6 7 GLY CA C 46.24 . . 26 6 7 GLY N N 110.688 . . 27 7 8 PHE H H 8.597 . . 28 7 8 PHE C C 177.409 . . 29 7 8 PHE CA C 60.554 . . 30 7 8 PHE CB C 38.624 . . 31 7 8 PHE N N 121.189 . . 32 8 9 THR H H 8.13 . . 33 8 9 THR C C 176.35 . . 34 8 9 THR CA C 66.081 . . 35 8 9 THR CB C 67.962 . . 36 8 9 THR N N 113.67 . . 37 9 10 ARG H H 7.713 . . 38 9 10 ARG C C 178.816 . . 39 9 10 ARG CA C 59.018 . . 40 9 10 ARG CB C 28.976 . . 41 9 10 ARG N N 121.08 . . 42 10 11 ILE H H 7.518 . . 43 10 11 ILE C C 179.01 . . 44 10 11 ILE CA C 63.995 . . 45 10 11 ILE CB C 36.805 . . 46 10 11 ILE N N 119.484 . . 47 11 12 ILE H H 7.518 . . 48 11 12 ILE C C 178.31 . . 49 11 12 ILE CA C 63.932 . . 50 11 12 ILE CB C 36.596 . . 51 11 12 ILE N N 119.484 . . 52 12 13 LYS H H 7.873 . . 53 12 13 LYS C C 179.431 . . 54 12 13 LYS CA C 58.769 . . 55 12 13 LYS CB C 31.28 . . 56 12 13 LYS N N 119.98 . . 57 13 14 ALA H H 7.777 . . 58 13 14 ALA CA C 54.098 . . 59 13 14 ALA CB C 17.408 . . 60 13 14 ALA N N 122.297 . . 61 14 15 ALA H H 7.856 . . 62 14 15 ALA C C 178.16 . . 63 14 15 ALA CA C 53.404 . . 64 14 15 ALA CB C 17.68 . . 65 14 15 ALA N N 119.666 . . 66 15 16 GLY H H 7.821 . . 67 15 16 GLY C C 175.065 . . 68 15 16 GLY CA C 45.95 . . 69 15 16 GLY N N 104.326 . . 70 16 17 TYR H H 7.619 . . 71 16 17 TYR C C 176.023 . . 72 16 17 TYR CA C 58.677 . . 73 16 17 TYR CB C 38.265 . . 74 16 17 TYR N N 119.919 . . 75 17 18 SER H H 7.909 . . 76 17 18 SER C C 174.912 . . 77 17 18 SER CA C 58.493 . . 78 17 18 SER CB C 64.394 . . 79 17 18 SER N N 114.862 . . 80 18 19 TRP H H 8.363 . . 81 18 19 TRP C C 178.869 . . 82 18 19 TRP CA C 58.795 . . 83 18 19 TRP CB C 28.873 . . 84 18 19 TRP N N 123.394 . . 85 19 20 LYS H H 8.053 . . 86 19 20 LYS C C 178.979 . . 87 19 20 LYS CA C 58.823 . . 88 19 20 LYS CB C 31.17 . . 89 19 20 LYS N N 119.371 . . 90 20 21 GLY H H 7.853 . . 91 20 21 GLY C C 175.473 . . 92 20 21 GLY CA C 45.974 . . 93 20 21 GLY N N 107.77 . . 94 21 22 LEU H H 7.85 . . 95 21 22 LEU C C 177.694 . . 96 21 22 LEU CA C 56.913 . . 97 21 22 LEU CB C 41.067 . . 98 21 22 LEU N N 122.836 . . 99 22 23 ARG H H 7.773 . . 100 22 23 ARG C C 177.308 . . 101 22 23 ARG CA C 58.047 . . 102 22 23 ARG CB C 29.497 . . 103 22 23 ARG N N 118.716 . . 104 23 24 ALA H H 7.694 . . 105 23 24 ALA C C 179.025 . . 106 23 24 ALA CA C 53.748 . . 107 23 24 ALA CB C 17.4 . . 108 23 24 ALA N N 121.072 . . 109 24 25 ALA H H 7.795 . . 110 24 25 ALA C C 178.604 . . 111 24 25 ALA CA C 53.98 . . 112 24 25 ALA CB C 17.606 . . 113 24 25 ALA N N 120.42 . . 114 25 26 TRP H H 7.755 . . 115 25 26 TRP C C 176.99 . . 116 25 26 TRP CA C 58.733 . . 117 25 26 TRP CB C 28.981 . . 118 25 26 TRP N N 117.083 . . 119 26 27 ILE H H 7.472 . . 120 26 27 ILE C C 176.347 . . 121 26 27 ILE CA C 62.303 . . 122 26 27 ILE CB C 36.934 . . 123 26 27 ILE N N 117.073 . . 124 27 28 ASN H H 7.682 . . 125 27 28 ASN C C 175.896 . . 126 27 28 ASN CA C 54.112 . . 127 27 28 ASN CB C 38.993 . . 128 27 28 ASN N N 118.07 . . 129 28 29 GLU H H 8.052 . . 130 28 29 GLU CA C 56.928 . . 131 28 29 GLU CB C 28.852 . . 132 28 29 GLU N N 119.755 . . 133 29 30 ALA C C 178.31 . . 134 30 31 ALA H H 7.856 . . 135 30 31 ALA C C 178.244 . . 136 30 31 ALA CA C 53.404 . . 137 30 31 ALA CB C 17.68 . . 138 30 31 ALA N N 119.666 . . 139 31 32 PHE H H 7.442 . . 140 31 32 PHE C C 176.147 . . 141 31 32 PHE CA C 58.539 . . 142 31 32 PHE CB C 38.226 . . 143 31 32 PHE N N 114.892 . . 144 32 33 ARG H H 7.567 . . 145 32 33 ARG C C 177.697 . . 146 32 33 ARG CA C 57.26 . . 147 32 33 ARG CB C 29.739 . . 148 32 33 ARG N N 118.243 . . 149 33 34 GLN H H 7.773 . . 150 33 34 GLN C C 179.369 . . 151 33 34 GLN CA C 56.82 . . 152 33 34 GLN CB C 29.499 . . 153 33 34 GLN N N 118.716 . . 154 34 35 GLU H H 8.23 . . 155 34 35 GLU C C 177.876 . . 156 34 35 GLU CA C 58.051 . . 157 34 35 GLU CB C 31.844 . . 158 34 35 GLU N N 119.819 . . 159 35 36 GLY H H 8.26 . . 160 35 36 GLY C C 175.117 . . 161 35 36 GLY CA C 47.384 . . 162 35 36 GLY N N 107.15 . . 163 36 37 VAL H H 7.647 . . 164 36 37 VAL CA C 66.323 . . 165 36 37 VAL CB C 30.455 . . 166 36 37 VAL N N 120.277 . . 167 37 38 ALA C C 178.807 . . 168 37 38 ALA CA C 55.388 . . 169 37 38 ALA CB C 17.54 . . 170 38 39 VAL H H 7.579 . . 171 38 39 VAL C C 177.694 . . 172 38 39 VAL CA C 66.384 . . 173 38 39 VAL CB C 30.418 . . 174 38 39 VAL N N 115.497 . . 175 39 40 LEU H H 7.729 . . 176 39 40 LEU C C 178.723 . . 177 39 40 LEU CA C 57.939 . . 178 39 40 LEU CB C 40.586 . . 179 39 40 LEU N N 118.831 . . 180 40 41 LEU H H 8.287 . . 181 40 41 LEU C C 178.316 . . 182 40 41 LEU CA C 57.841 . . 183 40 41 LEU CB C 40.439 . . 184 40 41 LEU N N 118.16 . . 185 41 42 ALA H H 7.912 . . 186 41 42 ALA C C 179.583 . . 187 41 42 ALA CA C 55.321 . . 188 41 42 ALA CB C 17.347 . . 189 41 42 ALA N N 120.741 . . 190 42 43 VAL H H 8.144 . . 191 42 43 VAL C C 178.09 . . 192 42 43 VAL CA C 67.39 . . 193 42 43 VAL CB C 30.35 . . 194 42 43 VAL N N 118.039 . . 195 43 44 VAL H H 8.171 . . 196 43 44 VAL C C 178.692 . . 197 43 44 VAL CA C 67.503 . . 198 43 44 VAL CB C 30.265 . . 199 43 44 VAL N N 120.104 . . 200 44 45 ILE H H 8.484 . . 201 44 45 ILE C C 178.47 . . 202 44 45 ILE CA C 65.894 . . 203 44 45 ILE CB C 36.929 . . 204 44 45 ILE N N 119.752 . . 205 45 46 ALA H H 8.656 . . 206 45 46 ALA C C 179.431 . . 207 45 46 ALA CA C 54.925 . . 208 45 46 ALA CB C 18.03 . . 209 45 46 ALA N N 120.965 . . 210 46 47 CYS H H 7.752 . . 211 46 47 CYS C C 173.343 . . 212 46 47 CYS CA C 63.27 . . 213 46 47 CYS CB C 27.435 . . 214 46 47 CYS N N 113.711 . . 215 47 48 TRP H H 8.066 . . 216 47 48 TRP C C 177.085 . . 217 47 48 TRP CA C 58.666 . . 218 47 48 TRP CB C 30.415 . . 219 47 48 TRP N N 121.423 . . 220 48 49 LEU H H 7.526 . . 221 48 49 LEU C C 176.818 . . 222 48 49 LEU CA C 55.037 . . 223 48 49 LEU CB C 43.769 . . 224 48 49 LEU N N 116.327 . . 225 49 50 ASP H H 8.911 . . 226 49 50 ASP C C 175.217 . . 227 49 50 ASP CA C 52.926 . . 228 49 50 ASP CB C 38.868 . . 229 49 50 ASP N N 123.257 . . 230 50 51 VAL H H 6.745 . . 231 50 51 VAL C C 174.82 . . 232 50 51 VAL CA C 58 . . 233 50 51 VAL CB C 34.488 . . 234 50 51 VAL N N 112.811 . . 235 51 52 ASP H H 7.766 . . 236 51 52 ASP C C 175.219 . . 237 51 52 ASP CA C 53.083 . . 238 51 52 ASP CB C 41.36 . . 239 51 52 ASP N N 118.463 . . 240 52 53 ALA H H 8.342 . . 241 52 53 ALA C C 178.925 . . 242 52 53 ALA CA C 55.68 . . 243 52 53 ALA CB C 18.211 . . 244 52 53 ALA N N 122 . . 245 53 54 ILE H H 7.591 . . 246 53 54 ILE C C 177.853 . . 247 53 54 ILE CA C 65.107 . . 248 53 54 ILE CB C 36.21 . . 249 53 54 ILE N N 116.586 . . 250 54 55 THR H H 8.021 . . 251 54 55 THR CA C 67.693 . . 252 54 55 THR CB C 66.792 . . 253 54 55 THR N N 118.33 . . 254 55 56 ARG C C 178.873 . . 255 56 57 VAL H H 6.936 . . 256 56 57 VAL C C 179.034 . . 257 56 57 VAL CA C 66.789 . . 258 56 57 VAL CB C 30.45 . . 259 56 57 VAL N N 116.478 . . 260 57 58 LEU H H 7.947 . . 261 57 58 LEU C C 180.378 . . 262 57 58 LEU CA C 57.842 . . 263 57 58 LEU CB C 41.496 . . 264 57 58 LEU N N 123.026 . . 265 58 59 LEU H H 8.336 . . 266 58 59 LEU C C 179.657 . . 267 58 59 LEU CA C 57.874 . . 268 58 59 LEU CB C 39.664 . . 269 58 59 LEU N N 121.062 . . 270 59 60 ILE H H 7.804 . . 271 59 60 ILE C C 178.054 . . 272 59 60 ILE CA C 65.461 . . 273 59 60 ILE CB C 38.404 . . 274 59 60 ILE N N 117.048 . . 275 60 61 SER H H 9.237 . . 276 60 61 SER C C 177.379 . . 277 60 61 SER CA C 62.653 . . 278 60 61 SER CB C 62.646 . . 279 60 61 SER N N 116.271 . . 280 61 62 SER H H 7.935 . . 281 61 62 SER C C 177.519 . . 282 61 62 SER CA C 61.645 . . 283 61 62 SER CB C 62.646 . . 284 61 62 SER N N 115.872 . . 285 62 63 VAL H H 7.046 . . 286 62 63 VAL C C 178.109 . . 287 62 63 VAL CA C 65.155 . . 288 62 63 VAL CB C 30.532 . . 289 62 63 VAL N N 118.906 . . 290 63 64 MET H H 8.242 . . 291 63 64 MET C C 179.397 . . 292 63 64 MET CA C 57.165 . . 293 63 64 MET CB C 30.314 . . 294 63 64 MET N N 119.989 . . 295 64 65 LEU H H 8.165 . . 296 64 65 LEU C C 178.837 . . 297 64 65 LEU CA C 57.938 . . 298 64 65 LEU CB C 39.536 . . 299 64 65 LEU N N 121.108 . . 300 65 66 VAL H H 6.936 . . 301 65 66 VAL C C 177.474 . . 302 65 66 VAL CA C 66.789 . . 303 65 66 VAL CB C 30.345 . . 304 65 66 VAL N N 116.478 . . 305 66 67 MET H H 6.931 . . 306 66 67 MET CA C 58.072 . . 307 66 67 MET CB C 32.406 . . 308 66 67 MET N N 116.516 . . 309 67 68 ILE C C 178.304 . . 310 68 69 VAL H H 7.982 . . 311 68 69 VAL C C 177.866 . . 312 68 69 VAL CA C 66.92 . . 313 68 69 VAL CB C 30.382 . . 314 68 69 VAL N N 116.436 . . 315 69 70 GLU H H 8.801 . . 316 69 70 GLU C C 179.876 . . 317 69 70 GLU CA C 59.076 . . 318 69 70 GLU CB C 28.066 . . 319 69 70 GLU N N 121.043 . . 320 70 71 ILE H H 8.395 . . 321 70 71 ILE C C 178.721 . . 322 70 71 ILE CA C 65.642 . . 323 70 71 ILE CB C 36.767 . . 324 70 71 ILE N N 122.605 . . 325 71 72 LEU H H 8.084 . . 326 71 72 LEU C C 179.186 . . 327 71 72 LEU CA C 58.113 . . 328 71 72 LEU CB C 41.072 . . 329 71 72 LEU N N 120.736 . . 330 72 73 ASN H H 8.831 . . 331 72 73 ASN C C 177.431 . . 332 72 73 ASN CA C 56.928 . . 333 72 73 ASN CB C 38.464 . . 334 72 73 ASN N N 117.737 . . 335 73 74 SER H H 8.344 . . 336 73 74 SER C C 177.244 . . 337 73 74 SER CA C 62.289 . . 338 73 74 SER CB C 62.646 . . 339 73 74 SER N N 116.626 . . 340 74 75 ALA H H 8.089 . . 341 74 75 ALA C C 178.806 . . 342 74 75 ALA CA C 55.334 . . 343 74 75 ALA CB C 17.275 . . 344 74 75 ALA N N 126.737 . . 345 75 76 ILE H H 7.832 . . 346 75 76 ILE C C 178.251 . . 347 75 76 ILE CA C 65.318 . . 348 75 76 ILE CB C 36.804 . . 349 75 76 ILE N N 118.51 . . 350 76 77 GLU H H 8.595 . . 351 76 77 GLU C C 178.35 . . 352 76 77 GLU CA C 59.843 . . 353 76 77 GLU CB C 28.73 . . 354 76 77 GLU N N 120.065 . . 355 77 78 ALA H H 7.612 . . 356 77 78 ALA C C 180.115 . . 357 77 78 ALA CA C 54.454 . . 358 77 78 ALA CB C 17.281 . . 359 77 78 ALA N N 119.968 . . 360 78 79 VAL H H 7.62 . . 361 78 79 VAL C C 177.775 . . 362 78 79 VAL CA C 66.077 . . 363 78 79 VAL CB C 30.376 . . 364 78 79 VAL N N 117.128 . . 365 79 80 VAL H H 8.102 . . 366 79 80 VAL C C 178.923 . . 367 79 80 VAL CA C 66.25 . . 368 79 80 VAL CB C 30.396 . . 369 79 80 VAL N N 118.797 . . 370 80 81 ASP H H 8.4 . . 371 80 81 ASP C C 177.922 . . 372 80 81 ASP CA C 56.613 . . 373 80 81 ASP CB C 39.678 . . 374 80 81 ASP N N 120.764 . . 375 81 82 ARG H H 7.529 . . 376 81 82 ARG CA C 57.018 . . 377 81 82 ARG CB C 30.315 . . 378 81 82 ARG N N 117.67 . . 379 82 83 ILE C C 174.514 . . 380 82 83 ILE CA C 59.775 . . 381 83 84 GLY H H 7.994 . . 382 83 84 GLY C C 174.504 . . 383 83 84 GLY CA C 43.518 . . 384 83 84 GLY N N 109.198 . . 385 84 85 SER H H 8.152 . . 386 84 85 SER C C 175.513 . . 387 84 85 SER CA C 59.291 . . 388 84 85 SER CB C 63.199 . . 389 84 85 SER N N 115.757 . . 390 85 86 GLU H H 8.328 . . 391 85 86 GLU C C 178.119 . . 392 85 86 GLU CA C 56.823 . . 393 85 86 GLU CB C 28.927 . . 394 85 86 GLU N N 122.181 . . 395 86 87 TYR H H 7.591 . . 396 86 87 TYR CA C 63.284 . . 397 86 87 TYR CB C 37.721 . . 398 86 87 TYR N N 118.4 . . 399 88 89 GLU C C 175.813 . . 400 89 90 LEU H H 8.044 . . 401 89 90 LEU CA C 58.093 . . 402 89 90 LEU CB C 39.483 . . 403 89 90 LEU N N 115.928 . . 404 90 91 SER C C 176.064 . . 405 91 92 GLY H H 7.975 . . 406 91 92 GLY C C 175.434 . . 407 91 92 GLY CA C 46.629 . . 408 91 92 GLY N N 108.959 . . 409 92 93 ARG H H 7.802 . . 410 92 93 ARG C C 178.014 . . 411 92 93 ARG CA C 58.448 . . 412 92 93 ARG CB C 29.416 . . 413 92 93 ARG N N 121.364 . . 414 93 94 ALA H H 7.971 . . 415 93 94 ALA C C 179.514 . . 416 93 94 ALA CA C 55.282 . . 417 93 94 ALA CB C 18.038 . . 418 93 94 ALA N N 121.056 . . 419 94 95 LYS H H 7.601 . . 420 94 95 LYS C C 179.515 . . 421 94 95 LYS CA C 59.049 . . 422 94 95 LYS CB C 31.41 . . 423 94 95 LYS N N 116.324 . . 424 95 96 ASP H H 8.415 . . 425 95 96 ASP C C 179.369 . . 426 95 96 ASP CA C 56.833 . . 427 95 96 ASP CB C 39.891 . . 428 95 96 ASP N N 121.633 . . 429 96 97 MET H H 8.23 . . 430 96 97 MET C C 177.876 . . 431 96 97 MET CA C 58.051 . . 432 96 97 MET CB C 31.889 . . 433 96 97 MET N N 119.819 . . 434 97 98 GLY H H 8.26 . . 435 97 98 GLY C C 176.279 . . 436 97 98 GLY CA C 47.384 . . 437 97 98 GLY N N 107.15 . . 438 98 99 SER H H 7.854 . . 439 98 99 SER C C 177.324 . . 440 98 99 SER CA C 61.723 . . 441 98 99 SER CB C 62.684 . . 442 98 99 SER N N 114.455 . . 443 99 100 ALA H H 8.028 . . 444 99 100 ALA C C 179.055 . . 445 99 100 ALA CA C 54.092 . . 446 99 100 ALA CB C 16.887 . . 447 99 100 ALA N N 125.426 . . 448 100 101 ALA H H 7.936 . . 449 100 101 ALA C C 179.263 . . 450 100 101 ALA CA C 55.465 . . 451 100 101 ALA CB C 16.699 . . 452 100 101 ALA N N 119.884 . . 453 101 102 VAL H H 7.33 . . 454 101 102 VAL C C 177.755 . . 455 101 102 VAL CA C 66.396 . . 456 101 102 VAL CB C 30.82 . . 457 101 102 VAL N N 117.291 . . 458 102 103 LEU H H 7.726 . . 459 102 103 LEU C C 179.012 . . 460 102 103 LEU CA C 58.148 . . 461 102 103 LEU CB C 40.396 . . 462 102 103 LEU N N 119.481 . . 463 103 104 ILE H H 8.266 . . 464 103 104 ILE C C 177.518 . . 465 103 104 ILE CA C 64.822 . . 466 103 104 ILE CB C 35.818 . . 467 103 104 ILE N N 117.18 . . 468 104 105 ALA H H 7.977 . . 469 104 105 ALA C C 179.941 . . 470 104 105 ALA CA C 55.865 . . 471 104 105 ALA CB C 16.432 . . 472 104 105 ALA N N 122.179 . . 473 105 106 ILE H H 8.103 . . 474 105 106 ILE C C 179.141 . . 475 105 106 ILE CA C 63.933 . . 476 105 106 ILE CB C 35.891 . . 477 105 106 ILE N N 117.18 . . 478 106 107 ILE H H 7.609 . . 479 106 107 ILE C C 177.417 . . 480 106 107 ILE CA C 66.611 . . 481 106 107 ILE CB C 36.671 . . 482 106 107 ILE N N 117.891 . . 483 107 108 VAL H H 8.376 . . 484 107 108 VAL C C 179.144 . . 485 107 108 VAL CA C 66.912 . . 486 107 108 VAL CB C 30.368 . . 487 107 108 VAL N N 118.308 . . 488 108 109 ALA H H 8.082 . . 489 108 109 ALA CA C 56.161 . . 490 108 109 ALA CB C 15.939 . . 491 108 109 ALA N N 126.871 . . 492 111 112 THR H H 8.302 . . 493 111 112 THR CA C 68.42 . . 494 111 112 THR N N 116.899 . . 495 112 113 TRP C C 178.547 . . 496 113 114 CYS H H 8.699 . . 497 113 114 CYS C C 176.983 . . 498 113 114 CYS CA C 64.883 . . 499 113 114 CYS CB C 26.785 . . 500 113 114 CYS N N 115.842 . . 501 114 115 ILE H H 8.519 . . 502 114 115 ILE C C 178.932 . . 503 114 115 ILE CA C 65.887 . . 504 114 115 ILE CB C 36.772 . . 505 114 115 ILE N N 116.935 . . 506 115 116 LEU H H 7.992 . . 507 115 116 LEU C C 180.297 . . 508 115 116 LEU CA C 57.341 . . 509 115 116 LEU CB C 40.295 . . 510 115 116 LEU N N 116.267 . . 511 116 117 LEU H H 8.422 . . 512 116 117 LEU C C 178.82 . . 513 116 117 LEU CA C 56.532 . . 514 116 117 LEU CB C 40.368 . . 515 116 117 LEU N N 117.641 . . 516 117 118 TRP H H 8.198 . . 517 117 118 TRP C C 178.654 . . 518 117 118 TRP CA C 60.641 . . 519 117 118 TRP CB C 28.878 . . 520 117 118 TRP N N 122.812 . . 521 118 119 SER H H 8.031 . . 522 118 119 SER C C 176.008 . . 523 118 119 SER CA C 60.268 . . 524 118 119 SER CB C 62.647 . . 525 118 119 SER N N 110.86 . . 526 119 120 HIS H H 7.776 . . 527 119 120 HIS C C 175.392 . . 528 119 120 HIS CA C 57.233 . . 529 119 120 HIS CB C 29.499 . . 530 119 120 HIS N N 118.762 . . 531 120 121 PHE H H 8.014 . . 532 120 121 PHE C C 175.089 . . 533 120 121 PHE CA C 58.246 . . 534 120 121 PHE CB C 39.512 . . 535 120 121 PHE N N 118.159 . . 536 121 122 GLY H H 7.61 . . 537 121 122 GLY CA C 46.049 . . 538 121 122 GLY N N 114.282 . . stop_ save_